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The changing of an enzymes shape as the substrate binds to the active site is called the?
The changing of an enzyme's shape as the substrate binds to the active site is called the "induced fit" model. This model suggests that the enzyme undergoes a conformational change to better accommodate the substrate, enhancing the enzyme's ability to catalyze the reaction. This interaction increases the specificity and efficiency of the enzyme's activity.
What does enzymes functions depend on?
The function of an enzyme is dependent on the shape of the enzyme. The structure and shape determines what the enzyme can do.
What can effect how the enzyme and substrate come together?
Factors such as temperature, pH, substrate concentration, and the presence of inhibitors or activators can affect how enzymes and substrates come together. Changes in these factors can alter the shape and activity of enzymes, impacting their ability to bind with substrates and catalyze reactions.
What is the effect of phosphorylation on enzyme activity?
Phosphorylation of an enzyme can either activate or inhibit its activity, depending on the specific enzyme and the site of phosphorylation. Addition of a phosphate group can change the shape or conformation of the enzyme, affecting its ability to bind substrates or cofactors. These changes can lead to either an increase or decrease in enzymatic activity.
How enzyme structure makes an enzyme very specific?
Enzymes are proteins, which are made up of amino acids. Each enzyme has a different sequence of amino acids and changing even one amino acid will mean that the tertiary structure of the enzyme will be lost and so will it's active site. As enzymes are substrate specific, only a certain substrate will bind to its active site, due to its amino acid sequence determining the shape of the active site.
What else can effect how an enzyme works by changing the enzyme's shape can the reaction still take place?
invalid question!
The changing of an enzymes shape as the substrate binds to the active site is called the?
The changing of an enzyme's shape as the substrate binds to the active site is called the "induced fit" model. This model suggests that the enzyme undergoes a conformational change to better accommodate the substrate, enhancing the enzyme's ability to catalyze the reaction. This interaction increases the specificity and efficiency of the enzyme's activity.
What does enzymes functions depend on?
The function of an enzyme is dependent on the shape of the enzyme. The structure and shape determines what the enzyme can do.
What can effect how the enzyme and substrate come together?
Factors such as temperature, pH, substrate concentration, and the presence of inhibitors or activators can affect how enzymes and substrates come together. Changes in these factors can alter the shape and activity of enzymes, impacting their ability to bind with substrates and catalyze reactions.
Why are balancing things like temperature and acidity so important to living things?
Enzymes are protiens. If you get the balance of pH or temperature outof wack, you can change the shape of the enzyme. Changing the shape of the said enzyme damages the protein, so it cannot do its job. This is called denaturing.
How do pH levels affected enzyme?
It disrupts an enzymes shape and structure.
What effects does acid have on ezyme?
Acids can denature enzymes and make them less active or completely inactive. Denaturation causes a change in the three-dimensional structure of an enzyme which can affect the function of the enzyme.
What can effect the shape of an enzyme molecule?
Temperature
What is the effect of heat on enzymes?
Heat can denature enzymes, causing them to lose their shape and therefore their function. At low temperatures, heat can increase the rate of enzyme activity, but at high temperatures, enzymes can become inactive due to the disruption of their protein structure.
What do acids and bases do to enzymes?
Acids and bases can denature enzymes by disrupting their shape and changing the active site where substrates bind. This alteration can prevent enzymes from catalyzing reactions effectively. pH changes can also affect the ionization of amino acid side chains, influencing enzyme activity.
Describe the chemical compositions and configuration of enzymes and discuss the factors that modify enzymes structure and function?
Enzymes are composed of amino acids, and have different bonds such as a hydrogen bond which maintains the enzyme's shape. Factors such as temperature and pH have an effect upon the enzymes structure. Enzymes have slower rates of reaction when the temperature is below the enzymes optimum temperature. This is due to the fact that hydrogen bonds are stronger at lower temperatures meaning that the enzyme is less flexible and so, using the induced fit theory, this means that the substrate is less able to fit into the enzymes active site meaning less substrate is broken down therefore the rate of reaction is much less than it would be at the enzymes optimum temperature. When the temperature also exceeds the enzymes optimum temperature the rate of reaction is again slower that it would be at the optimum temperature, this is due to the high temperature causing the hydrogen bonds to be broken, meaning the enzyme can be denatured, and there is a point where the enzymes are unable to "renature" (when temp is returned to optimum) because too many hydrogen bonds would have been broken. pH is a factor which also affects the enzymes structure, by changing the pH from the enzymes optimum pH you are then causing there to be a change in the enzymes structure and molecular shape. pH can in turn strengthen or weaken the intermolecular forces like the hydrogen bonds. Competitive inhibitors can also alter the enzymes function. Competitive inhibitors have a molecular shape which is similar to the shape of the substrate; This means that they can occupy the enzymes active site meaning that they compete with the substrate for an available active site. The difference between the concentration of the competitive inhibitor and the substrate determines the effect upon the enzyme activity, if the competitive inhibitors concentration is highest the effect of the substrate is lessened. The inhibitor is not permenantly bound to the enzymes active site, so when it leaves another molecule may take its place, either another inhibitor or substrate. Sooner or later all of the substrate will occupy active sites of enzymes, but if the inhibitor concentration is higher this may take some time. Non-competitive inhibitors can also effect the enzyme activity by attaching themselves to the enzyme, but not at the active site. This attachment means the enzyme's active site may under-go a shape change meaning that the substrate may not fit into it, causing the effect of the enzyme to be lowered as less substrate can be broken down. Non-competitive inhibitors may be permanent. Hope this helps you, even if it is very slightly.
What characteristic allows enzymes to function a specific way?
Each enzyme has a characteristic shape
